Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus

EMBO Journal

Volumn 15, Issue 18, 1996, Pages 4789-4797

  Baba, Tadashi ^a   Schneewind, Olaf ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Bacteriocin; Lysostaphin; Peptidoglycan; Protein targeting; Staphylococci

Indexed keywords

BACTERIOCIN; PEPTIDOGLYCAN;

ANTIBIOTIC BIOSYNTHESIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL KILLING; CELL WALL; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING; STAPHYLOCOCCUS AUREUS; TARGET CELL;

EID: 0029790464     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00859.x     Document Type: Article

References (35)

1. Benedetti, H., Frenette, M., Baty, D., Knibiehler, M., Pattus, F. and Lazdunski, C. (1991) Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement. J. Mol. Biol., 217, 429-439.
2. Browder, H.P., Zygmunt, W.A., Young, J.R. and Tavormina, P.A. (1965) Lysostaphin: enzymatic mode of action. Biochem. Biophys. Res. Commun., 19, 383-389.
3. Dehart, H.P., Heath, H.E., Heath, L.S., Leblanc, P.A. and Sloan, G.L. (1995) The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol., 61, 1475-1479.
4. Díaz, E., García, E., Ascaso, C., Méndez, E., López, R. and García, J.L. (1989) Subcellular localization of the major pneumococcal autolysin: a peculiar mechanism of secretion in Escherichia coli. J. Biol. Chem., 264, 1238-1244.
5. Garrido, M.C., Herrero, M., Kolter, R. and Moreno, F. (1988) The export of the DNA replication inhibitor microcin B17 provides immunity for the host cell. EMBO J., 7, 1853-1862.
6. Ghuysen, J.-M. (1968) Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol. Rev., 32, 425-464.
7. Hash, J.H. (1963) Purification and properties of staphylolytic enzymes from Chalaropsis sp. Arch. Biochem. Biophys., 102, 379-388.
8. Heath, H.E., Heath, L.S., Nitterauer, J.D., Rose, K.E. and Sloan, G.L. (1989) Plasmid-encoded lysostaphin endopeptidase resistance of Staphylococcus simulans biovar staphylolyticus. Biochem. Biophys. Res. Commun., 160, 1106-1109.
9. Heinrich, P., Rosenstein, R., Bohmer, M., Sonner, P. and Götz, F. (1987) The molecular organization of the lysostaphin gene and its sequences repeated in tandem. Mol. Gen. Genet., 209, 563-569.
10. Jack, R.W., Tagg, J.R. and Ray, B. (1995) Bacteriocins of gram-positive bacteria. Microbiol. Rev., 59, 171-200.
11. Jones, C.L. and Khan, S.A. (1986) Nucleotide sequence of the enterotoxin B gene from Staphylococcus aureus. J. Bacteriol., 166, 29-33.
12. Kline, S.A., Harpe, J. and Blackburn, P. (1994) A colorimetric microtiter plate assay for lysostaphin using a hexaglycine substrate. Anal. Biochem., 217, 329-331.
13. Kolter, R. (1992) Genetics of ribosomally synthesized peptide antibiotics. Annu. Rev. Microbiol., 46, 141-163.
14. Navarre, W.W. and Schneewind, O. (1994) Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol. Microbiol., 14, 115-121.
15. Novick, R.P. (1991) Genetic systems in staphylococci. Methods Enzymol., 204, 587-636.
16. Novick, R.P. and Richmond, M.H. (1965) Nature and interactions of the genetic elements governing penicillinase synthesis in Staphylococcus aureus. J. Bacteriol., 90, 467-480.
17. Oshida, T., Sugai, M., Komatsuzawa, H., Hong, Y.-M., Suginaka, H. and Tomaz, A. (1995) A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc. Natl Acad. Sci. USA, 92, 285-289.
18. Pattus, F., Massotte, D., Wilmsen, H.U., Lakey, J., Tsernoglou, D., Tucker, A. and Parker, M.W. (1990) Colicins: prokaryotic killer-pores. Experientia, 46, 180-192.
19. Pilsl, H. and Braun, V. (1995) Evidence that the immunity protein inactivates colicin 5 immediately prior to the formation of the transmembrane channel. J. Bacteriol., 177, 6966-6972.
20. Recsei, P.A., Gruss, A.D. and Novick, R.P. (1987) Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans. Proc. Natl Acad. Sci. USA, 84, 1127-1131.
21. Sanz, J.M., Díaz, E. and García, J.L. (1992) Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases. Mol. Microbiol., 6, 921-931.
22. Schindler, C.A. and Schuhardt, V.T. (1964) Lysostaphin: a new bacteriolytic agent for the staphylococcus. Proc. Natl Acad. Sci. USA, 51, 414-421.
23. Schleifer, K.H. and Kandler, O. (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev., 36, 407-477.
24. Schneewind, O., Model, P. and Fischetti, V.A. (1992) Sorting of protein A to the staphylococcal cell wall. Cell, 70, 267-281.
25. Schneewind, O., Mihaylova-Petkov, D. and Model, P. (1993) Cell wall sorting signals in surface protein of gram-positive bacteria. EMBO J., 12, 4803-4811.
26. Schneewind, O., Fowler, A. and Faull, K.F. (1995) Structure of the cell wall anchor of surface proteins in Staphylococcus aureus. Science, 268, 103-106.
27. Sloan, G.L., Smith, E.C. and Lancaster, J.H. (1977) Lysostaphin endopeptidase-catalyzed transpeptidation reactions of the imino-transfer type. Biochem. J., 167, 293-296.
28. Smith, D.B. and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-40.
29. Strominger, J.L., Izaki, K., Matsuhashi, M. and Tipper, D.J. (1967) Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Fed. Proc., 26, 9-18.
30. Tweten, R.K. and Iandolo, J.J. (1983) Transport and processing of staphylococcal enterotoxin B. J. Bacteriol., 153, 297-303.
31. van de Rijn, I. and Kessler, R.E. (1980) Growth characteristics of group A streptococci in a new chemically defined medium. Infect. Immunol., 27, 444-448.
32. Wang, A., Wilkinson, B.J. and Jayaswal, R.K. (1991a) Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Gene, 102, 105-109.
33. Wang, P.-Z., Projan, S.J. and Novick, R.P. (1991b) Nucleotide sequence of β-lactamase regulatory genes from staphylococcal plasmid p1258. Nucleic Acids Res., 19, 4000.
34. Yamada, S., Sugai, M., Komatsuzawa, H., Nakashima, S., Oshida, T., Matsumoto, A. and Suginaka, H. (1996) An autolysin ring associated with cell separation of Staphylococcus aureus. J. Bacteriol., 178, 1565-1571.
35. Zhu, X.L., Ohta, Y., Jordan, F. and Inouye, M. (1989) Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature, 339, 483.